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Database: UniProt
Entry: P0ABE1
LinkDB: P0ABE1
Original site: P0ABE1 
ID   BCCP_SHIFL              Reviewed;         156 AA.
AC   P0ABE1; P02905;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JAN-2019, entry version 87.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase;
DE            Short=BCCP;
GN   Name=accB; OrderedLocusNames=SF3293, S3510;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
DR   EMBL; AE005674; AAN44757.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18568.1; -; Genomic_DNA.
DR   RefSeq; NP_709050.1; NC_004337.2.
DR   RefSeq; WP_000354622.1; NZ_UIQL01000035.1.
DR   ProteinModelPortal; P0ABE1; -.
DR   SMR; P0ABE1; -.
DR   EnsemblBacteria; AAN44757; AAN44757; SF3293.
DR   EnsemblBacteria; AAP18568; AAP18568; S3510.
DR   GeneID; 1027068; -.
DR   KEGG; sfl:SF3293; -.
DR   KEGG; sfx:S3510; -.
DR   PATRIC; fig|198214.7.peg.3901; -.
DR   eggNOG; ENOG4105KM4; Bacteria.
DR   eggNOG; COG0511; LUCA.
DR   HOGENOM; HOG000008875; -.
DR   KO; K02160; -.
DR   OMA; IKSPIIG; -.
DR   OrthoDB; 1938042at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR00531; BCCP; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   3: Inferred from homology;
KW   Biotin; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN         1    156       Biotin carboxyl carrier protein of
FT                                acetyl-CoA carboxylase.
FT                                /FTId=PRO_0000146811.
FT   DOMAIN       73    156       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   MOD_RES     122    122       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   156 AA;  16687 MW;  05FFDCB912A683A3 CRC64;
     MDIRKIKKLI ELVEESGISE LEISEGEESV RISRAAPAAS FPVMQQAYAA PMMQQPAQSN
     AAAPATVPSM EAPAAAEISG HIVRSPMVGT FYRTPSPDAK AFIEVGQKVN VGDTLCIVEA
     MKMMNQIEAD KSGTVKAILV ESGQPVEFDE PLVVIE
//
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